3QAZ: IL-2 mutant D10 ternary complex
IL-2 mutant D10 ternary complex. Determined by X-ray diffraction at 3.8 Å resolution. Released 11 Apr 2012.
- Method
- X-ray diffraction
- Resolution
- 3.8 Å
- Organism
- Homo sapiens
- Chains
- 36
- Atoms
- 51,562
- Mol. weight
- 791.56 kDa
- Ligands
- NAG
- Released
- 11 Apr 2012
Explore 3QAZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3QAZ contains 220 α-helices and 450 β-strands across 36 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain a: 7 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-37 | 3 | |
| β-strand | 39-43 | 5 | 2 |
| β-strand | 47-51 | 5 | 2 |
| α-helix | 54-56 | 3 | |
| β-strand | 64-69 | 6 | 3 |
| β-strand | 78 | 1 | 3 |
| β-strand | 82-85 | 4 | 2 |
| β-strand | 90-95 | 6 | 2 |
| α-helix | 97-99 | 3 | |
| α-helix | 105 | 1 | |
| β-strand | 106-111 | 6 | 3 |
| β-strand | 119-124 | 6 | 3 |
| α-helix | 126-128 | 3 | |
| β-strand | 130-131 | 2 | 2 |
| α-helix | 132-135 | 4 | |
| β-strand | 136-142 | 7 | 4 |
| β-strand | 148-153 | 6 | 4 |
| β-strand | 161-169 | 9 | 5 |
| β-strand | 176-180 | 5 | 5 |
| β-strand | 186-188 | 3 | 4 |
| β-strand | 197-205 | 9 | 5 |
| α-helix | 217-219 | 3 | |
| β-strand | 222-223 | 2 | 5 |
Chain A: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-28 | 22 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-70 | 8 | |
| α-helix | 82-95 | 14 | |
| β-strand | 107-112 | 6 | 1 |
| α-helix | 114-131 | 18 | |
Chain b: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-28 | 22 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44 | 1 | 10 |
| α-helix | 45-46 | 2 | |
| β-strand | 47 | 1 | 11 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-61 | 5 | |
| α-helix | 63-70 | 8 | |
| α-helix | 82-94 | 13 | |
| β-strand | 107 | 1 | 11 |
| β-strand | 112 | 1 | 10 |
| α-helix | 114-130 | 17 | |
Chain B: 5 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 6 |
| β-strand | 17-23 | 7 | 6 |
| β-strand | 33-39 | 7 | 7 |
| β-strand | 46-49 | 4 | 7 |
| β-strand | 51-52 | 2 | 6 |
| β-strand | 57-63 | 7 | 6 |
| β-strand | 78-86 | 9 | 7 |
| β-strand | 89-98 | 10 | 7 |
| α-helix | 100-102 | 3 | |
| β-strand | 104 | 1 | 6 |
| α-helix | 106-109 | 4 | |
| β-strand | 110-117 | 8 | 8 |
| β-strand | 122-127 | 6 | 8 |
| α-helix | 133-135 | 3 | |
| β-strand | 139-146 | 8 | 9 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 9 |
| β-strand | 166-169 | 4 | 8 |
| β-strand | 177-186 | 10 | 9 |
| α-helix | 194-200 | 7 | |
| β-strand | 201-204 | 4 | 9 |
Chain c: 3 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-12 | 5 | 16 |
| β-strand | 17-23 | 7 | 16 |
| β-strand | 33-39 | 7 | 17 |
| β-strand | 46-49 | 4 | 17 |
| β-strand | 51-52 | 2 | 16 |
| β-strand | 57-63 | 7 | 16 |
| β-strand | 78-86 | 9 | 17 |
| β-strand | 89-98 | 10 | 17 |
| α-helix | 100-102 | 3 | |
| β-strand | 104 | 1 | 16 |
| α-helix | 106-109 | 4 | |
| β-strand | 110-117 | 8 | 18 |
| β-strand | 122-127 | 6 | 18 |
| β-strand | 140-146 | 7 | 19 |
| β-strand | 157-160 | 4 | 19 |
| β-strand | 166-168 | 3 | 18 |
| β-strand | 177-178 | 2 | 20 |
| β-strand | 179-185 | 7 | 19 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-204 | 2 | 20 |
Chain C: 7 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-38 | 4 | |
| β-strand | 39-43 | 5 | 12 |
| β-strand | 47-51 | 5 | 12 |
| β-strand | 64-69 | 6 | 13 |
| α-helix | 77 | 1 | |
| β-strand | 78-79 | 2 | 13 |
| α-helix | 80 | 1 | |
| β-strand | 83-85 | 3 | 12 |
| β-strand | 90-96 | 7 | 12 |
| α-helix | 97-99 | 3 | |
| β-strand | 106-111 | 6 | 13 |
| β-strand | 119-124 | 6 | 13 |
| α-helix | 126-128 | 3 | |
| β-strand | 130-131 | 2 | 12 |
| α-helix | 132-135 | 4 | |
| β-strand | 136-144 | 9 | 14 |
| β-strand | 147-153 | 7 | 14 |
| β-strand | 161-169 | 9 | 15 |
| β-strand | 176-180 | 5 | 15 |
| β-strand | 185-188 | 4 | 14 |
| β-strand | 197-205 | 9 | 15 |
| α-helix | 217-221 | 5 | |
| β-strand | 222-223 | 2 | 15 |
Chain d: 4 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-37 | 3 | |
| β-strand | 39-43 | 5 | 22 |
| β-strand | 47-51 | 5 | 22 |
| β-strand | 64-68 | 5 | 23 |
| β-strand | 78-79 | 2 | 23 |
| β-strand | 82-85 | 4 | 22 |
| β-strand | 90-95 | 6 | 22 |
| β-strand | 106-111 | 6 | 23 |
| β-strand | 119-124 | 6 | 23 |
| α-helix | 126-129 | 4 | |
| β-strand | 130-131 | 2 | 22 |
| α-helix | 132-135 | 4 | |
| β-strand | 136-139 | 4 | 24 |
| β-strand | 142 | 1 | 25 |
| β-strand | 148-150 | 3 | 25 |
| β-strand | 151-153 | 3 | 24 |
| β-strand | 161-167 | 7 | 26 |
| β-strand | 176-180 | 5 | 26 |
| β-strand | 186-188 | 3 | 25 |
| β-strand | 198-205 | 8 | 26 |
| α-helix | 215-219 | 5 | |
| β-strand | 222-223 | 2 | 26 |
Chain D: 8 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-28 | 19 | |
| α-helix | 36-41 | 6 | |
| β-strand | 44-47 | 4 | 21 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-70 | 8 | |
| α-helix | 75-77 | 3 | |
| α-helix | 82-94 | 13 | |
| β-strand | 107-112 | 6 | 21 |
| α-helix | 114-130 | 17 | |
28 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Interleukin-2 | A, D, G, J, M, P, S, V, Y, b, e, h | protein | 136 | Homo sapiens | P60568 (AlphaFold model) |
| Interleukin-2 receptor subunit beta | B, E, H, K, N, Q, T, W, Z, c, f, i | protein | 217 | Homo sapiens | P14784 (AlphaFold model) |
| Cytokine receptor common subunit gamma | C, F, I, L, O, R, U, X, a, d, g, j | protein | 202 | Homo sapiens | P31785 (AlphaFold model) |
Sequence of entity 1 (A, D, G, J, M, P, S, V, Y, b, e, h), FASTA
>3QAZ_1 Interleukin-2 (chains A, D, G, J, M, P, S, V, Y, b, e, h)
ADPAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQ
CLEEELKPLEEVLNLAHSKNFHFDPRDVVSNINVFVLELKGSETTFMCEYADETATIVEF
LNRWITFCQSIISTLT
Sequence of entity 2 (B, E, H, K, N, Q, T, W, Z, c, f, i), FASTA
>3QAZ_2 Interleukin-2 receptor subunit beta (chains B, E, H, K, N, Q, T, W, Z, c, f, i)
ADPAVQGTSQFTCFYNSRAQISCVWSQDGALQDTSCQVHAWPDRRRWQQTCELLPVSQAS
WACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHV
ETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQ
YEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDT
Sequence of entity 3 (C, F, I, L, O, R, U, X, a, d, g, j), FASTA
>3QAZ_3 Cytokine receptor common subunit gamma (chains C, F, I, L, O, R, U, X, a, d, g, j)
ADPPLPEVQCFVFNVEYMNCTWQSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEIT
SGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLEL
NWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCG
SAQHWSEWSHPIHWGSNTSKEN
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 54 |
Primary citation
Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'. Levin, A.M., Bates, D.L., Ring, A.M. et al. Nature (2012) 484:529-533. DOI 10.1038/nature10975 · PubMed
Other PDB entries of the same protein (UniProt P60568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8SOZ 1.64 Å, Structure of the complex formed by human interleukin-2 and scFv 602
- 8SOW 1.71 Å, Structure of the complex formed by human interleukin-2 and scFv F10
- 7M2G 1.79 Å, INTERLEUKIN-2 (human) mutant P65K, C125S
- 4NEJ 1.92 Å, Small molecular fragment bound to crystal contact interface of Interleukin-2
- 4NEM 1.93 Å, Small molecular fragment bound to crystal contact interface of Interleukin-2
- 1M48 1.95 Å, Crystal Structure of Human IL-2 Complexed with (R)-N-[2-[1-(Aminoiminomethyl)-3-piperidin…
- 5LQB 1.95 Å, Complex structure of human IL2 mutant, Proleukin, with Fab fragment of NARA1 antibody
- 1M47 1.99 Å, Crystal Structure of Human Interleukin-2
- 1M49 2.0 Å, Crystal Structure of Human Interleukin-2 Complexed with SP-1985
- 1M4B 2.15 Å, Crystal Structure of Human Interleukin-2 K43C Covalently Modified at C43 with…
- 1M4A 2.18 Å, Crystal Structure of Human Interleukin-2 Y31C Covalently Modified at C31 with…
- 1NBP 2.2 Å, Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With…
Browse structure collections
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